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Merck

D1315

Sigma-Aldrich

DT Diaphorase (NQO1) human

lyophilized powder, recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Sinónimos:

DTD, NQO1, Quinone reductase

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About This Item

Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

assay

≥90% (SDS-PAGE)

form

lyophilized powder

specific activity

≥100 units/mg protein

mol wt

monomer 31000

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... NQO1(1728)

Application

Human DT diaphorase has been used in a study to assess the development of novel quinone phosphorodiamidate prodrugs. Human DT diaphorase has also been used to investigate its crystal structure for the development of a model for its interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).

Biochem/physiol Actions

DT-diaphorase, also referred to as NAD(P)H:(quinone-acceptor) oxidoreductase, is involved in the reductive activation process of several cytotoxic antitumor quinones and nitrobenzenes. It catalyzes the two-electron reduction of quinones and quinonoid compounds to hydroquinones, using either NADH or NADPH as the electron donor. The flavoenzyme contains one mole of FAD per mole of enzyme.
NQO1 is a cytosolic homodimeric FAD-dependent enzyme that catalyses the reduction of a broad range of cytotoxic quinones resulting in protection from cellular oxidative stress. Oxidative stress may also enhance NQO1-mediated protection of p53 and p73 against proteasomal degredation. The highly Inducible expression of NQO1 is controlled by the Nrf2-Keap1/ARE pathway and appears to be affected by changes in susceptibility to oxidative stress. During Oxygen/glucose deprivation, NQO1 appears to be involved in AMPK-induced cancer cell death. NQO1 has been observed to be overexpressed in several types of solid tumors, including breast, pancreas, lung and colon cancer.
Shown to activate quinone based anti-tumor agents in vivo. Suitable for conjugation to carrier molecules.

Unit Definition

One unit will reduce 1.0 μmole cytochrome C per min/mg in the presence of menadione substrate at 37 °C.

inhibitor

Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Eeva-Riikka Vehniäinen et al.
Aquatic toxicology (Amsterdam, Netherlands), 116-117, 102-108 (2012-04-10)
Ethoxyresorufin-O-deethylase (EROD) activity is a biomarker of exposure to planar aromatic hydrocarbons, and it is often measured from the S9 fraction. The effect of the liver S9 fraction of seven boreal freshwater fish species on the fluorescence of resorufin was
S Chen et al.
The Journal of biological chemistry, 272(3), 1437-1439 (1997-01-17)
DT-diaphorase (EC 1.6.99.2), also referred to as NAD(P)H:(quinone-acceptor) oxidoreductase, is involved in the reductive activation process of several cytotoxic antitumor quinones and nitrobenzenes. It has been observed in our and other laboratories that the rat enzyme is significantly more effective
C Flader et al.
Journal of medicinal chemistry, 43(16), 3157-3167 (2000-08-24)
A series of naphthoquinone and benzimidazolequinone phosphorodiamidates has been synthesized and studied as potential cytotoxic prodrugs activated by DT-diaphorase. Reduction of the quinone moiety in the target compounds was expected to provide a pathway for expulsion of the phosphoramide mustard
Yang Yang et al.
Journal of experimental & clinical cancer research : CR, 33, 14-14 (2014-02-07)
NAD (P) H: quinone oxidoreductase 1 (NQO1) is a xenobiotic metabolizing enzyme that detoxifies chemical stressors and antioxidants, providing cytoprotection in normal tissues. However, high-level expression of NQO1 has been correlated with numerous human malignancies, suggesting a role in carcinogenesis
David Siegel et al.
Frontiers in pharmacology, 13, 1015642-1015642 (2022-11-22)
The stress induced protein NQO1 can participate in a wide range of biological pathways which are dependent upon the interaction of NQO1 with protein targets. Many of the protein-protein interactions involving NQO1 have been shown to be regulated by the

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